X-ray structural, functional and computational studies of the O 2 -sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Chemical Communications Année : 2018

X-ray structural, functional and computational studies of the O 2 -sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster

X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe-4S] cluster.

Anne Volbeda
J. Mouesca
  • Fonction : Auteur
M. Roessler
  • Fonction : Auteur
A. Parkin
  • Fonction : Auteur
F. Armstrong
  • Fonction : Auteur

Résumé

The crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni-Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype.

Dates et versions

hal-01828168 , version 1 (03-07-2018)

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Citer

Anne Volbeda, J. Mouesca, Claudine Darnault, M. Roessler, A. Parkin, et al.. X-ray structural, functional and computational studies of the O 2 -sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster. Chemical Communications, 2018, 54 (52), pp.7175 - 7178. ⟨10.1039/c8cc02896f⟩. ⟨hal-01828168⟩
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